Abstract
Conjugation of ISG15 inhibits replication of several viruses. Here, using an expression system for assaying human and mouse ISG15 conjugations (ISGylations), we have demonstrated that vaccinia virus E3 protein binds and antagonizes human and mouse ISG15 modification. To study ISGylation importance in poxvirus infection, we used a mouse model that expresses deconjugating proteases. Our results indicate that ISGylation restricts in vitro replication of the vaccinia virus VVΔE3L mutant but unconjugated ISG15 is crucial to counteract the inflammatory response produced after VVΔE3L infection.
Publication types
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Research Support, N.I.H., Extramural
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Research Support, Non-U.S. Gov't
MeSH terms
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Animals
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Cytokines / antagonists & inhibitors
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Cytokines / genetics
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Cytokines / metabolism*
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Histological Techniques
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Humans
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Intracellular Signaling Peptides and Proteins / metabolism
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Mice
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Mice, Knockout
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Mutation / genetics
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Peptide Hydrolases / metabolism
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Poxviridae Infections / metabolism*
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Poxviridae Infections / pathology*
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RNA-Binding Proteins / metabolism*
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Ubiquitins / antagonists & inhibitors
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Ubiquitins / genetics
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Ubiquitins / metabolism*
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Viral Proteins / metabolism*
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Virus Replication / genetics*
Substances
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Cytokines
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E3L protein, Vaccinia virus
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HERC5 protein, human
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Intracellular Signaling Peptides and Proteins
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RNA-Binding Proteins
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Ubiquitins
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Viral Proteins
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ISG15 protein, human
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Peptide Hydrolases